Disease relevance of gamma-Thio-ATP

• Adenosine-5'-O-(3-thiotriphosphate) as an affinity probe for studying leader RNA's transcribed by vesicular stomatitis virus [1].
• The fluorescence of the LexA protein, the common repressor of the SOS system in Escherichia coli decreases by about 30% upon incubation with the RecA protein, and its cofactors ATP [or its non-hydrolysable analogue adenosine-5'-O-(3-thiotriphosphate), ATP gamma S] Mg2+ and single-stranded DNA [2].

High impact information on gamma-Thio-ATP

• In addition, HsRad51 bound gamma-thio-ATP and formed stable presynaptic complexes that promoted renaturation as rapidly as RecA, but the recombinant human protein catalyzed neither strand exchange nor homologous pairing of a single strand with duplex DNA in the presence of the ATP analog [3].
• Our results suggest that the binding of ATP to alpha-crystallin and not its hydrolysis is required for all these effects, as replacement of ATP by its nonhydrolyzable analogue adenosine-5'-O-(3-thiotriphosphate), tetralithium salt, reproduced all the results faithfully [4].
• This is the reason why Mg2+ inhibits Ca2+ binding, and this inhibition is removed in the presence of adenosine-5'-O-(3-thiotriphosphate) which drives Mg2+ into the catalytic site [5].
• RecA protein-mediated DNA strand exchange is affected minimally by changes in reaction conditions (dilution, pH shift, or addition of small amounts of adenosine-5'-O-(3-thiotriphosphate) that have large and demonstrable effects on recA protein association, dissociation, or both [6].
• 2. Shortening was also dependent on [ATP] but could be increased at low [ATP] by pretreatment with adenosine-5'-O-(3-thiotriphosphate) (ATP gamma S), which suggests that myosin phosphorylation was more sensitive to low substrate concentrations than was cross-bridge cycling [7].

Biological context of gamma-Thio-ATP

• The mechanism of activation apparently requires ATP hydrolysis since adenosine-5'-O-(3-thiotriphosphate) not only fails to support the reaction but also inhibits activation promoted by ATP [8].
• Stress-induced apoptosis of mesangial cells is reduced by the stable ATP analogue, gamma-thio-ATP, and this inhibitory effect is reversed in the presence of LY 294002 [9].

Anatomical context of gamma-Thio-ATP

• 2. Extracellular adenosine-5'-O-(3-thiotriphosphate) (ATPgammaS; 100 microM) activated ICl,ATP in both atrial and ventricular myocytes [10].
• We have used saturation transfer electron paramagnetic resonance (ST-EPR) to measure the microsecond rotational motion of actin-bound myosin heads in spin-labeled myofibrils in the presence of the ATP analogs AMPPNP (5'-adenylylimido-diphosphate) and ATP gamma S (adenosine-5'-O-(3-thiotriphosphate)) [11].
• Adenosine-5'-O-(3-thiotriphosphate) binding to human neutrophils. Evidence for a common nucleotide receptor [12].
• Intact hepatocytes respond to extracellular ATP, adenosine-5'-O-(3-thiotriphosphate) (ATP gamma S), ADP and weakly to guanosine-5'-triphosphate (GTP), but not to other purine nucleotides (GDP or AMP) [13].
• Here we analyzed whether nucleoside diphosphokinase present in these membranes and capable of forming GTP[S] from GDP and adenosine-5'-O-(3-thiotriphosphate) (ATP[S]) can contribute to nucleotide regulation of agonist receptor binding [14].

Associations of gamma-Thio-ATP with other chemical compounds

• Nuclear chalcone synthase in vitro transcripts were affinity-labelled with gamma-thio-ATP, gamma-thio-GTP or beta-thio-ATP, and purified by chromatography on a mercury Sepharose affinity column [15].

Gene context of gamma-Thio-ATP

• UTP and ATP were very effective analogues to activate p38-MAPK, whereas ADP and gamma-thio-ATP had only moderate activating effects [16].
• UTP, ATP and gamma-thio-ATP are the only compounds capable of activating PKB [9].

Analytical, diagnostic and therapeutic context of gamma-Thio-ATP

• RNA chains (less than 5 S) initiated with adenosine-5'-O-(3-thiotriphosphate) can be isolated by affinity chromatography on mercury-agarose columns used in these experiments [1].
• Primer extension and subsequent PCR amplification of these in vitro transcripts revealed gamma-thio-ATP-dependent, but no beta-thio-ATP-dependent, signals, although affinity labelling of overall in vitro transcripts still occurred with beta-thio-ATP [15].

References